1qcl

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

PREDICTED STRUCTURE OF HUMAN MYELIN BASIC PROTEIN.

spinqualitylabelsall models 1qcl Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed A computational model of myelin basic protein (MBP) has been constructed based on the premise of a phylogenetically conserved beta-sheet backbone and on electron microscopical three-dimensional reconstructions. Many residues subject to post-translational modification (phosphorylation, methylation, or conversion of arginines to citrullines) were located in loop regions and thus accessible to modifying enzymes. The triproline segment (residues 99-101) is fully exposed on the back surface of the protein in a long crossover connection between two parallel beta-strands. The proximity of this region to the underlying beta-sheet suggests that post-translational modifications here might have potential synergistic effects on the entire structure. Post-translational modifications that lead to a reduced surface charge could result first in a weakened attachment to the myelin membrane rather than in a gross conformational change of the protein itself. Such mechanisms could be operative in demyelinating diseases such as multiple sclerosis. Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis.,Ridsdale RA, Beniac DR, Tompkins TA, Moscarello MA, Harauz G J Biol Chem. 1997 Feb 14;272(7):4269-75. PMID:9020143 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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